9x1i

Structure of endo-beta-N-acetylglucosaminidase HS

spinqualitylabelsall models 9x1i, resolution 1.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9x1i is a 2 chain structure with sequence from Human oral metagenome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.81Å Ligands: GOL, K, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The crystal structure of endo-beta-N-acetylglucosaminidase HSalpha (Endo HSalpha) was determined at 1.8 A resolution, revealing that the enzyme is composed of five distinct domains. Domains I to III adopt a fold that is conserved among GH85 enzymes, with catalytic residues Asn216, Glu218 and Tyr252 corresponding to conserved positions, while Tyr282 is newly implicated in catalysis based on the Endo HSalpha structure. A long loop unique to Endo HSalpha constricts the active site in domain I. Domain IV represents a novel structural element that is not observed in other GH85 enzymes. Its glycan-binding model and structural similarity to known sugar-binding domains play a role in substrate recognition. The minimal contacts with other domains allow it to remain flexible, accommodating bulky substrates at the active site. These features provide insights into the structural basis for substrate specificity and expand the structural diversity of the GH85 family. Crystal structure of endo-beta-N-acetylglucosaminidase HSalpha.,Kurauchi I, Okura K, Hosokawa C, Ito K, Miyahara I Acta Crystallogr F Struct Biol Commun. 2026 Mar 1;82(Pt 3):94-100. doi: , 10.1107/S2053230X26001214. Epub 2026 Feb 28. PMID:41784007 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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